1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
This is an abbreviated version!
For detailed information about 3,4-dihydroxyphenylacetate 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.15
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1.13.11.15
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extradiol
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catecholate
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4-nitrocatechol
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fuscum
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brevibacterium
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globiformis
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manganese-dependent
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ring-cleaving
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extradiol-cleaving
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second-sphere
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monoanionic
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hydroperoxo
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4-hydroxyphenylacetate
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superoxo
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alkylperoxo
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feiii-superoxo
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manganeseii
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ortho-dihydroxylated
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side-on
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crystallo
- 1.13.11.15
-
extradiol
-
catecholate
- 4-nitrocatechol
- fuscum
-
brevibacterium
- globiformis
-
manganese-dependent
-
ring-cleaving
-
extradiol-cleaving
-
second-sphere
-
monoanionic
-
hydroperoxo
- 4-hydroxyphenylacetate
-
superoxo
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alkylperoxo
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feiii-superoxo
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manganeseii
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ortho-dihydroxylated
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side-on
-
crystallo
Reaction
Synonyms
2,3-HPCD, 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, Bf 2,3-HPCD, DHPAO, Fe-HPCD, Fe-MndD, FeHPCD, homoprotocatechuate 2,3 dioxygenase, homoprotocatechuate 2,3-dioxygenase, homoprotocatechuate dioxygenase, HPADO, HPC 2,3-dioxygenase, HPC dioxygenase, HPCA 2,3-dioxygenase, HPCD, Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase, Mn-HPCD, Mn-MndD, MndD, MnHPCD, oxygenase, homoprotocatechuate 2,3-di-, PaDHPAO
ECTree
1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 1.13.11.15 - 3,4-dihydroxyphenylacetate 2,3-dioxygenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Fe(NH4)2(SO4)2
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activates at 0.5 mM, activation is enhanced by 10 mM DTT
Fe2+
Iron
Manganese
Mn
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wild-type enzyme amd mutant enzymes H200A and H200Q: 0.6 Mn per monomer. Mutant enzyme H200E: 0.3 Mn per monomer. Mutent enzyme H200N: 0.4 MN per monomer
Mn2+
NO
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NO binding to a non-heme enzyme containing manganese allows examination of the factors governing the formation and detection of the MIII-O2.- species in all forms of th enzyme. NO, and presumably O2, binding is sensitive to both the nature of the catecholic substrate present and the nature of the active-site amino acid residue at position 200, spectral analysis, overview
additional information
Fe2+
small model including only the most relevant parts of the residues, H155, H214, E267, Y257, directyl coordinated to Fe(II)
Fe2+
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Fe2+-containing homoprotocatechuate 2,3-dioxygenase, FeHPCD, activates O2 to catalyze the aromatic ring opening of homoprotocatechuate
Fe2+
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FeHPCD, substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites
Fe2+
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the catalytic Fe2+ is active site bound, electron transfer from the chelated aromatic substrate through the Fe2+ to O2 gives both substrates radical character promoting reaction between the substrates to form an alkylperoxo intermediate as the first step in aromatic ring cleavage
Fe2+
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0.71 mol/subunit, dependent on, a mononuclear non-heme ferrous ion, Fe(II), is the metal cofactor
Iron
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4-5 gatom of iron per mol of enzyme, most of the iron is involved in the association of the subunits, at least 1 gatom of iron is at the active site
Iron
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the non-heme bound-iron is in the ferrous state and is essential for activity
Manganese
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enzyme is dependent on manganese, the conserved residues H155, H1214 and E266 ligate manganese
additional information
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the enzyme is fully functional using metals with a redox potential range spanning 1.15 V. Recombinant extradiol dioxygenase homoprotocatechuate 2,3-dioxygenase functions with the same kcat, and kcat/KmO2 values within error when the Fe2+ is replaced by Mn2+. It exhibits even higher kcat and KmO2 values when Co2+ is substituted
additional information
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the enzyme requires Fe2+ for catalysis, but Mn2+ can be substituted (MnHPCD) with essentially no change in the steady-state kinetic parameters, spectral analysis, overview
additional information
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apoPaDHPAO cannot be restored by substitution with either Mn(II) or Co(II), although the two metal ions can bind to apoPaDHPAO, Fe(II) is the native and mandatory metal ion for PaDHPAO. 10 mM DTT alone does not activate the enzyme
